3b3q

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Revision as of 09:10, 23 January 2008

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spinqualitylabelsall models 3b3q, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of a synaptic adhesion complex

Overview

The heterophilic synaptic adhesion molecules neuroligins and neurexins are, essential for establishing and maintaining neuronal circuits by modulating, the formation and maturation of synapses. The neuroligin-neurexin adhesion, is Ca2+-dependent and regulated by alternative splicing. We report a, structure of the complex at a resolution of 2.4 A between the mouse, neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta, (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like), domain. The structure revealed a delicate neuroligin-neurexin assembly, mediated by a hydrophilic, Ca2+-mediated and solvent-supplemented, interface, rendering it capable of being modulated by alternative splicing, and other regulatory factors. Thermodynamic data supported a mechanism, wherein splicing site B of NL1 acts by modulating a salt bridge at the, edge of the NL1-NX1beta interface. Mapping neuroligin mutations implicated, in autism indicated that most such mutations are structurally, destabilizing, supporting deficient neuroligin biosynthesis and processing, as a common cause for this brain disorder.

About this Structure

3B3Q is a Protein complex structure of sequences from Homo sapiens and Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions., Chen X, Liu H, Shim AH, Focia PJ, He X, Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:18084303

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